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Notes: The authors compared the transformation potency of five Bcr-Abl kinase domain mutants. They found reproducible differences in the transformation potency of these five mutants, and they investigated whether these potencies could be explained by changes in kinase activity by performing in vitro kinase assays using a biotinylated peptide substrate. Assays were carried out using varying peptide substrate concentrations. The reactions were stopped, and aliquots of each reaction were transferred to the SAM2® Biotin Capture Membrane. Membranes were dried and phosphate incorporation was determined by scintillation counting. (3505)

Notes: Voltage-dependent and independent events regulate the activation of the Cav2.2 calcium channel in dorsal root ganglion neurons (DRG). The authors of this study synthesized a biotinylated tyrosine-containing peptide capable of crossing cell membranes. DRG neurons were treated in the presence of this peptide and then lysed. The lysates were applied to a SAM2 Biotin Capture Membrane to capture the biotinylated peptide, and tyrosine phosphorylation was measured. (3547)

Biochemistry37, 9827-9835.
Implication of DNA-dependent protein kinase in an early, essential, local phosphorylation event during end-joining of DNA double-strand breaks in vitro.1998

Gu, X.-Y., Weinfeld, M.A., Povirk, L.F.

Notes: The ability of wortmannin to inhibit DNA-dependent phosphorylation was determined with the SignaTECT® DNA-PK Assay System. Rather than counting the individual SAM2® Membrane squares, the authors exposed the membrane to film for a graphic display of the inhibition. (1081)

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